We demonstrate a dipolar-chemical shift correlation technique for sign-sensitive determination of the torsion angle in solid peptides and proteins under magic-angle spinning. The indirect dimension of the experiment is obtained by separate but synchronous evolution of the magnetization under the 15
Magnitudes and Orientations of the 15N Chemical Shift Tensor of [1-15N]-2′-Deoxyguanosine Determined on a Polycrystalline Sample by Two-Dimensional Solid-State NMR Spectroscopy
✍ Scribed by Gary A. Lorigan; Ronald McNamara; Roger A. Jones; Stanley J. Opella
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 72 KB
- Volume
- 140
- Category
- Article
- ISSN
- 1090-7807
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✦ Synopsis
The magnitudes and orientations of the 15 N chemical shift tensor of [1-15 N]-2-deoxyguanosine were determined from a polycrystalline sample using the two-dimensional PISEMA experiment. The magnitudes of the principal values of the 15 N chemical shift tensor of the N1 nitrogen of [1-15 N]-2-deoxyguanosine were found to be 11 ؍ 54 ppm, 22 ؍ 148 ppm, and 33 ؍ 201 ppm with respect to ( 15 NH 4 ) 2 SO 4 in aqueous solution. Comparisons of experimental and simulated two-dimensional powder pattern spectra show that 33N is approximately collinear with the N-H bond. The tensor orientation of 33N for N1 of [1-15 N]-2-deoxyguanosine is similar to the values obtained for the side chain residues of 15 N ⑀1 -tryptophan and 15 N -histidine even though the magnitudes differ significantly.
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